Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009739 | biological_process | response to gibberellin |
| A | 0009939 | biological_process | positive regulation of gibberellic acid mediated signaling pathway |
| A | 0010325 | biological_process | raffinose family oligosaccharide biosynthetic process |
| A | 0010331 | molecular_function | gibberellin binding |
| A | 0010476 | biological_process | gibberellin mediated signaling pathway |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0048444 | biological_process | floral organ morphogenesis |
| A | 0048530 | biological_process | fruit morphogenesis |
| A | 0071456 | biological_process | cellular response to hypoxia |
| A | 1905516 | biological_process | positive regulation of fertilization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GA3 A 345 |
| Chain | Residue |
| A | PHE27 |
| A | ASP243 |
| A | ARG244 |
| A | TYR247 |
| A | VAL319 |
| A | GLY320 |
| A | TYR322 |
| A | HOH364 |
| A | HOH458 |
| A | ARG35 |
| A | GLY115 |
| A | SER116 |
| A | TYR127 |
| A | ASP190 |
| A | SER191 |
| A | PHE238 |
| A | VAL239 |
Functional Information from PROSITE/UniProt
| site_id | PS01173 |
| Number of Residues | 17 |
| Details | LIPASE_GDXG_HIS Lipolytic enzymes "G-D-X-G" family, putative histidine active site. ILfFHGGSFahsSanSA |
| Chain | Residue | Details |
| A | ILE109-ALA125 | |
| site_id | PS01174 |
| Number of Residues | 13 |
| Details | LIPASE_GDXG_SER Lipolytic enzymes "G-D-X-G" family, putative serine active site. IfLAGDSSGGnIA |
| Chain | Residue | Details |
| A | ILE185-ALA197 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Motif: {"description":"Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole","evidences":[{"source":"UniProtKB","id":"Q5NUF3","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q0ZPV7","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU10038","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19037309","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZSI","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19037309","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZSH","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Motif: {"description":"DELLA motif","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Motif: {"description":"LEXLE motif","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Motif: {"description":"VHYNP motif","evidences":[{"evidenceCode":"ECO:0000255"}]} |
